Cloning, Expression, Purification, Crystallization and Preliminary X-Ray Crystallographic Analysis of C-12 Hydroxylase EryK from Saccharopolyspora erythraea

Autor: Steven G. Kendrew, Giuliano Sciara, Adriana E. Miele, Carmelinda Savino, Beatrice Vallone

Publikováno v: Protein and Peptide Letters
Protein and Peptide Letters, Bentham Science Publishers, 2008, 15 (10), pp.1138-1141. ⟨10.2174/092986608786071201⟩
Protein and peptide letters
15 (2008): 1138–1141. doi:10.2174/092986608786071201
info:cnr-pdr/source/autori:Savino,C.; Miele,A.E.; Sciara,G.; Kendrew,S.G.; Vallone,B./titolo:Cloning, epression, purification, crystallization and preliminary X-ray crystallographic analyis of C-12 Hydroxylase EryK from Saccharoplyspora erythraea/doi:10.2174%2F092986608786071201/rivista:Protein and peptide letters (Print)/anno:2008/pagina_da:1138/pagina_a:1141/intervallo_pagine:1138–1141/volume:15

Erythromycin A is produced by Saccharopolyspora erythraea via a secondary metabolic pathway using several steps including glycosylations and hydroxylations of the first macrolide intermediate 6-deoxyerythronolide B. Erythromycin C-12 hydroxylase (CYP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::620647e22ba6b56c47b902357dff914f
https://doi.org/10.2174/092986608786071201

Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate

Autor: Savino C, Montemiglio LC, Sciara G, Miele AE, Kendrew SG, Jemth P, Gianni S, Vallone B.

Publikováno v: The Journal of biological chemistry
284 (2009): 29170–29179. doi:10.1074/jbc.M109.003590
info:cnr-pdr/source/autori:Savino C; Montemiglio LC; Sciara G; Miele AE; Kendrew SG; Jemth P; Gianni S; Vallone B./titolo:Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate/doi:10.1074%2Fjbc.M109.003590/rivista:The Journal of biological chemistry (Print)/anno:2009/pagina_da:29170/pagina_a:29179/intervallo_pagine:29170–29179/volume:284

Cytochrome P450s are heme-containing proteins that catalyze the oxidative metabolism of many physiological endogenous compounds. Because of their unique oxygen chemistry and their key role in drug and xenobiotic metabolism, particular attention has b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::38a29ac4b78264b9b57e269e37b44a1f
https://publications.cnr.it/doc/11751

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